9UGG

PsdAB dimer (peptidisc sample)

9UGG の概要

• エントリーDOI: 10.2210/pdb9ugg/pdb
• EMDBエントリー: 64138
• 分子名称: Lantibiotic ABC transporter ATP-binding protein PsdA, Lantibiotic ABC transporter permease PsdB, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: abc transpoter, transport protein
• 由来する生物種: Bacillus sp. TSA-4; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 265181.45

構造登録者

He, Y.T.,Fan, W.J.,Shao, K.,Luo, M. (登録日: 2025-04-11, 公開日: 2026-04-15)

主引用文献

He, Y.,Fan, W.,Shi, J.,Gan, B.K.,Shao, K.,Zhu, F.,Hong, X.,Luo, M.
Cryo-EM structure of the Nisin resistance pump PsdAB reveals an unusual ABC transporter architecture.
Structure, 34:311-321.e5, 2026

PubMed Abstract: Bacteria have evolved diverse strategies to resist antimicrobial peptides, among them lipid II-targeting lantibiotics such as nisin. PsdAB, an ABC-type transporter regulated by the PsdRS two-component system, contributes to nisin resistance, though its structural and mechanistic basis have remained unclear. Here, we report the cryo-EM structure of Bacillus subtilis PsdAB, revealing a dimeric assembly with an unusually large central cavity at the TMD interface. Cross-linking studies confirm the dimeric nature of PsdAB both in vitro and in cells. Functional assays demonstrate that dimer-disrupting mutations compromise nisin resistance, highlighting the importance of dimerization for activity. Compared to canonical ABC transporter types, PsdAB adopts an atypical architecture comprising four NBDs and two TMDs arranged around a central cavity, which may accommodate lipid II. We propose that PsdAB represents a previously unrecognized ABC transporter class. These findings offer new insights into transporter-mediated lantibiotic resistance and suggest a potential mechanism of lipid II shielding.

PubMed: 41418778
DOI: 10.1016/j.str.2025.11.013

実験手法

ELECTRON MICROSCOPY (3.6 Å)